2MP0

Protein Phosphorylation upon a Fleeting Encounter

2MP0 の概要

• エントリーDOI: 10.2210/pdb2mp0/pdb
• NMR情報: BMRB: 19958
• 分子名称: Phosphoenolpyruvate-protein phosphotransferase, Glucose-specific phosphotransferase enzyme IIA component, PHOSPHITE ION (3 entities in total)
• 機能のキーワード: ein eiiaglc complex, transferase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46444.93

構造登録者

Xing, Q.,Yang, J.,Huang, P.,Zhang, W.,Tang, C. (登録日: 2014-05-08, 公開日: 2014-08-20, 最終更新日: 2024-05-01)

主引用文献

Xing, Q.,Huang, P.,Yang, J.,Sun, J.Q.,Gong, Z.,Dong, X.,Guo, D.C.,Chen, S.M.,Yang, Y.H.,Wang, Y.,Yang, M.H.,Yi, M.,Ding, Y.M.,Liu, M.L.,Zhang, W.P.,Tang, C.
Visualizing an ultra-weak protein-protein interaction in phosphorylation signaling.
Angew.Chem.Int.Ed.Engl., 53:11501-11505, 2014

PubMed Abstract: Proteins interact with each other to fulfill their functions. The importance of weak protein-protein interactions has been increasingly recognized. However, owing to technical difficulties, ultra-weak interactions remain to be characterized. Phosphorylation can take place via a K(D)≈25 mM interaction between two bacterial enzymes. Using paramagnetic NMR spectroscopy and with the introduction of a novel Gd(III)-based probe, we determined the structure of the resulting complex to atomic resolution. The structure accounts for the mechanism of phosphoryl transfer between the two enzymes and demonstrates the physical basis for their ultra-weak interaction. Further, molecular dynamics (MD) simulations suggest that the complex has a lifetime in the micro- to millisecond regimen. Hence such interaction is termed a fleeting interaction. From mathematical modeling, we propose that an ultra-weak fleeting interaction enables rapid flux of phosphoryl signal, providing a high effective protein concentration.

PubMed: 25131700
DOI: 10.1002/anie.201405976

実験手法

SOLUTION NMR